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Ion-pairs in proteins.

D J Barlow, J M Thornton

Journal of Molecular Biology

|August 25, 1983

Summary

This summary is machine-generated.

A new definition for ion-pairs in proteins reveals they are crucial for stabilizing tertiary structures. Most ion-pairs are exposed to solvent and not highly conserved unless functionally important.

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Area of Science:

Biochemistry
Structural Biology
Protein Science

Background:

Ion-pairs, interactions between oppositely charged residues, are vital for protein structure and function.
Understanding the precise role and characteristics of ion-pairs in globular proteins requires a clear definition and systematic analysis.

Purpose of the Study:

To derive a working definition for protein ion-pairs based on distance distributions of charged groups.
To analyze the properties and roles of ion-pairs in globular proteins.

Main Methods:

Analysis of distance distributions for charged groups in 38 proteins to establish a criterion for ion-pair identification (≤ 4 Å).
Systematic investigation of ion-pair characteristics including frequency, residue separation, secondary structure, side-chain flexibility, conformation, environment, and conservation.

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Main Results:

Approximately one-third of charged residues in proteins form ion-pairs.
76% of identified ion-pairs primarily stabilize tertiary protein structure.
Only 17% of ion-pairs are buried within the protein; conservation is low unless functionally significant.

Conclusions:

The derived definition provides a framework for studying ion-pairs in globular proteins.
Ion-pairs play a significant role in tertiary structure stabilization, with most being solvent-accessible and having low conservation unless functionally specified.